Biological membrane proteins have a large variety of functions, including acting as pumps, channels, valves, energy transducers, and mechanical, thermal, and electrical sensors, among many others. Membrane proteins play a role in many important cellular activities including energy conversion, cell signaling, cell-cell interactions, cell adhesion, cell migration, protein trafficking, viral fusion, neural synaptic activities and ion and metabolite transport. Membrane proteins are embedded in the lipid bilayer of the cell membrane and are comprised of both hydrophobic and hydrophilic moieties. Membranes comprising an artificial lipid bilayer with incorporated functional membrane proteins, such as ion channel peptides and transmembrane proteins are useful in a diverse range of technical applications. Since these proteins are nanometers in size and highly efficient, they are highly attractive for use in artificial devices. However, their natural lipid membrane environment suffers from shortcomings such as low strength, necessity of an aqueous environment, and susceptibility to chemical or bacterial degradation. Another common problem for such membranes is the need for stability of the membranes over time and against mechanical, electrical and chemical impacts.
Because membrane proteins possess both hydrophobic and hydrophilic regions, they are difficult to solubilize, extract and purify. One of the challenges posed by membrane proteins is that they are subject to rapid denaturation and/or aggregation in solution. Despite the availability of a wide range of surfactants, few provide increased and/or prolonged stability of membrane proteins in solution and/or in the membranes. Therefore, there remains a need in the art for surfactants capable of increasing the stability of membrane proteins. The present disclosure provides methods, compositions, kits and apparatuses to address these problems.